Evidence map›Paper›PMID 26457425›Full record

ArticleActa crystallographica. Section D, Biological crystallography2015

Structure of the novel monomeric glyoxalase I from Zea mays.

Gino L Turra, Romina B Agostini, Carolina M Fauguel, Daniel A Presello, Carlos S Andreo, Javier M González, Valeria A Campos-Bermudez

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 26% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Human Glyoxalase Gene Family in Health and Disease.Chemical research in toxicology · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Gino L TurraCentro de Estudios Fotosintéticos y Bioquímicos (CEFOBI-CONICET), Universidad Nacional de Rosario, Suipacha 531, S2002LRK Rosario, Argentina.
Romina B AgostiniCentro de Estudios Fotosintéticos y Bioquímicos (CEFOBI-CONICET), Universidad Nacional de Rosario, Suipacha 531, S2002LRK Rosario, Argentina.
Carolina M FauguelInstituto Nacional de Tecnología Agropecuaria (INTA), CC 31, B2700KXC Pergamino, Argentina.
Daniel A PreselloInstituto Nacional de Tecnología Agropecuaria (INTA), CC 31, B2700KXC Pergamino, Argentina.
Carlos S AndreoCentro de Estudios Fotosintéticos y Bioquímicos (CEFOBI-CONICET), Universidad Nacional de Rosario, Suipacha 531, S2002LRK Rosario, Argentina.
Javier M GonzálezProtein Crystallography Station, Bioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Valeria A Campos-BermudezCentro de Estudios Fotosintéticos y Bioquímicos (CEFOBI-CONICET), Universidad Nacional de Rosario, Suipacha 531, S2002LRK Rosario, Argentina.
National Agricultural Technology Institute · ARLos Alamos National Laboratory · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393
6 · The paper itself

Abstract

The glyoxalase system is ubiquitous among all forms of life owing to its central role in relieving the cell from the accumulation of methylglyoxal, a toxic metabolic byproduct. In higher plants, this system is upregulated under diverse metabolic stress conditions, such as in the defence response to infection by pathogenic microorganisms. Despite their proven fundamental role in metabolic stresses, plant glyoxalases have been poorly studied. In this work, glyoxalase I from Zea mays has been characterized both biochemically and structurally, thus reporting the first atomic model of a glyoxalase I available from plants. The results indicate that this enzyme comprises a single polypeptide with two structurally similar domains, giving rise to two lateral concavities, one of which harbours a functional nickel(II)-binding active site. The putative function of the remaining cryptic active site remains to be determined.

Indexed as

Amino Acid SequenceCatalytic DomainCloning, MolecularCrystallography, X-RayLactoylglutathione LyaseModels, MolecularMolecular Sequence DataNickelProtein ConformationSequence AlignmentZea maysLactoylglutathione LyaseNickelglyoxalasemaizemethylglyoxal

Identifiers

PMID26457425
PMCPMC4601366
OpenAlexW1894906253

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.